5end - Revision history

OCA at 12:51, 17 January 2024

2024-01-17T12:51:46Z

←Older revision		Revision as of 12:51, 17 January 2024
Line 3:		Line 3:
	<StructureSection load='5end' size='340' side='right'caption='[[5end]], [[Resolution\|resolution]] 2.55Å' scene=''>		<StructureSection load='5end' size='340' side='right'caption='[[5end]], [[Resolution\|resolution]] 2.55Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5end]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Vibch Vibch~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5END OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5END FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5end]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_cholerae_O1_biovar_El_Tor_str._N16961 Vibrio cholerae O1 biovar El Tor str. N16961]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5END OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5END FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>~~</td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.55Å</td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>fabG, VC_2021 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&~~id=~~243277 VIBCH])</td~~><~~/tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
-	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b></td><td class="sblockDat"><span class='plainlinks~~'>[https://en.wikipedia.org/wiki/3-oxoacyl-[acyl-carrier-protein]_reductase 3-oxoacyl-[acyl-carrier-protein] reductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.100 1.1.1.100] </~~span~~></td></tr>	+
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5end FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5end OCA], [https://pdbe.org/5end PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5end RCSB], [https://www.ebi.ac.uk/pdbsum/5end PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5end ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5end FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5end OCA], [https://pdbe.org/5end PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5end RCSB], [https://www.ebi.ac.uk/pdbsum/5end PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5end ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/FABG_VIBCH FABG_VIBCH]] Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis.	+	[https://www.uniprot.org/uniprot/FABG_VIBCH FABG_VIBCH] Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 28:		Line 27:
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Vibch~~]]	+	[[Category: Vibrio cholerae O1 biovar El Tor str. N16961]]
-	[[Category: Anderson~~, W F]]~~	+	[[Category: Anderson WF]]
-	~~[[Category: Structural genomic~~]]	+	[[Category: Cooper DR]]
-	[[Category: Cooper~~, D R~~]]	+	[[Category: Hou J]]
-	[[Category: Hou, J]]	+	[[Category: Minor W]]
-	[[Category: Minor, W]]	+	[[Category: Zheng H]]
-	[[Category: Zheng, H]]	+
-	~~[[Category: Beta-ketoacyl-acyl carrier protein reductase]]~~	+
-	~~[[Category: Csgid]]~~	+
-	~~[[Category: Fabg]]~~	+
-	~~[[Category: Oxidoreductase]]~~	+
-	~~[[Category: Vibrio cholerae~~]]	+

OCA at 10:10, 13 April 2022

2022-04-13T10:10:23Z

←Older revision		Revision as of 10:10, 13 April 2022
Line 3:		Line 3:
	<StructureSection load='5end' size='340' side='right'caption='[[5end]], [[Resolution\|resolution]] 2.55Å' scene=''>		<StructureSection load='5end' size='340' side='right'caption='[[5end]], [[Resolution\|resolution]] 2.55Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5end]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Vibch Vibch]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5END OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=5END FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5end]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibch Vibch]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5END OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5END FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">fabG, VC_2021 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243277 VIBCH])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">fabG, VC_2021 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243277 VIBCH])</td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/3-oxoacyl-[acyl-carrier-protein]_reductase 3-oxoacyl-[acyl-carrier-protein] reductase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.100 1.1.1.100] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/3-oxoacyl-[acyl-carrier-protein]_reductase 3-oxoacyl-[acyl-carrier-protein] reductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.100 1.1.1.100] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=5end FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5end OCA], [~~http~~://pdbe.org/5end PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5end RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5end PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5end ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5end FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5end OCA], [https://pdbe.org/5end PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5end RCSB], [https://www.ebi.ac.uk/pdbsum/5end PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5end ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/FABG_VIBCH FABG_VIBCH]] Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis.	+	[[https://www.uniprot.org/uniprot/FABG_VIBCH FABG_VIBCH]] Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 07:06, 22 April 2020

2020-04-22T07:06:10Z

←Older revision		Revision as of 07:06, 22 April 2020
Line 1:		Line 1:

	==Crystal structure of beta-ketoacyl-acyl carrier protein reductase (FabG)(Q152A) from Vibrio cholerae==		==Crystal structure of beta-ketoacyl-acyl carrier protein reductase (FabG)(Q152A) from Vibrio cholerae==
-	<StructureSection load='5end' size='340' side='right' caption='[[5end]], [[Resolution\|resolution]] 2.55Å' scene=''>	+	<StructureSection load='5end' size='340' side='right'caption='[[5end]], [[Resolution\|resolution]] 2.55Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5end]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5END OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5END FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5end]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Vibch Vibch]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5END OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5END FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">fabG, VC_2021 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243277 VIBCH])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3-oxoacyl-[acyl-carrier-protein]_reductase 3-oxoacyl-[acyl-carrier-protein] reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.100 1.1.1.100] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3-oxoacyl-[acyl-carrier-protein]_reductase 3-oxoacyl-[acyl-carrier-protein] reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.100 1.1.1.100] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5end FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5end OCA], [http://pdbe.org/5end PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5end RCSB], [http://www.ebi.ac.uk/pdbsum/5end PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5end FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5end OCA], [http://pdbe.org/5end PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5end RCSB], [http://www.ebi.ac.uk/pdbsum/5end PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5end ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 19:		Line 20:
	</div>		</div>
	<div class="pdbe-citations 5end" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5end" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Beta-hydroxyacyl-acyl carrier protein dehydratase 3D structures\|Beta-hydroxyacyl-acyl carrier protein dehydratase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Vibch]]
	[[Category: Anderson, W F]]		[[Category: Anderson, W F]]
	[[Category: Structural genomic]]		[[Category: Structural genomic]]

OCA at 10:24, 26 February 2016

2016-02-26T10:24:54Z

←Older revision		Revision as of 10:24, 26 February 2016
Line 1:		Line 1:
		+
	==Crystal structure of beta-ketoacyl-acyl carrier protein reductase (FabG)(Q152A) from Vibrio cholerae==		==Crystal structure of beta-ketoacyl-acyl carrier protein reductase (FabG)(Q152A) from Vibrio cholerae==
	<StructureSection load='5end' size='340' side='right' caption='[[5end]], [[Resolution\|resolution]] 2.55Å' scene=''>		<StructureSection load='5end' size='340' side='right' caption='[[5end]], [[Resolution\|resolution]] 2.55Å' scene=''>

OCA at 12:42, 23 December 2015

2015-12-23T12:42:28Z

←Older revision		Revision as of 12:42, 23 December 2015
Line 1:		Line 1:
-	'''~~Unreleased~~ structure'''	+	==Crystal structure of beta-ketoacyl-acyl carrier protein reductase (FabG)(Q152A) from Vibrio cholerae==
		+	<StructureSection load='5end' size='340' side='right' caption='[[5end]], [[Resolution\|resolution]] 2.55Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5end]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5END OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5END FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3-oxoacyl-[acyl-carrier-protein]_reductase 3-oxoacyl-[acyl-carrier-protein] reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.100 1.1.1.100] </span></td></tr>
		+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5end FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5end OCA], [http://pdbe.org/5end PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5end RCSB], [http://www.ebi.ac.uk/pdbsum/5end PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/FABG_VIBCH FABG_VIBCH]] Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	beta-ketoacyl-(acyl carrier protein) reductase (FabG) catalyzes the key reductive reaction in the elongation cycle of fatty acid synthesis (FAS), which is a vital metabolic pathway in bacteria and a promising target for new antibiotic development. The activation of the enzyme is usually linked to the formation of a catalytic triad and cofactor binding, and crystal structures of FabG from different organisms have been captured in either active or inactive conformations. However, the structural elements which enable activation of FabG require further exploration. Here we report structural, enzymatic, and binding studies of vcFabG, the FabG protein found in the causative agent of cholera, Vibrio cholerae. vcFabG exists predominantly as a dimer in solution and is able to self-associate to form tetramers, which is the state seen in the crystal structure. The formation of the tetramer may be promoted by the presence of the cofactor NADP(H). The transition between dimeric and tetrameric states of vcFabG is related to changes in the conformations of the alpha4/alpha5 helices on the dimer-dimer interface. Two glycine residues adjacent to the dimer interface (G92 and G141) are identified as the hinge for the conformational changes, while the catalytic tyrosine (Y155) and a glutamine residue that forms hydrogen bonds to both loops beta4-alpha4 and beta5-alpha5 (Q152) stabilize the active conformation. The functions of the aforementioned residues were confirmed by the binding and enzymatic assays for the corresponding mutants. IMPORTANCE: This paper describes structural, enzymatic, and binding studies of FabG from Vibrio cholera. In this work we dissect the structural elements responsible for the activation of vcFabG. The structural information provided here is essential for the development of antibiotics specifically targeting bacteria FabG, especially for the multi-drug resistant strains of V. cholerae.

-	~~The entry 5end is ON HOLD~~	+	Dissecting the structural elements for the activation of beta-ketoacyl-(acyl carrier protein) reductase from Vibrio cholerae.,Hou J, Zheng H, Chruszcz M, Zimmerman MD, Shumilin IA, Osinski T, Demas M, Grimshaw S, Minor W J Bacteriol. 2015 Nov 9. pii: JB.00360-15. PMID:26553852<ref>PMID:26553852</ref>

-	~~Authors: Hou~~, J.~~, Cooper, D~~.R.~~, Zheng, H.,~~ Anderson, W.F~~., Minor, W., Center for~~ Structural ~~Genomics of Infectious Diseases (CSGID)~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~Description~~: ~~Crystal structure of beta-ketoacyl-acyl carrier protein reductase (FabG)(Q152A) from Vibrio cholerae~~	+	<div class="pdbe-citations 5end" style="background-color:#fffaf0;"></div>
-	[[Category: ~~Unreleased Structures~~]]	+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Anderson, W F]]
		+	[[Category: Structural genomic]]
		+	[[Category: Cooper, D R]]
		+	[[Category: Hou, J]]
		+	[[Category: Minor, W]]
	[[Category: Zheng, H]]		[[Category: Zheng, H]]
-	[[Category: ~~Minor, W~~]]	+	[[Category: Beta-ketoacyl-acyl carrier protein reductase]]
-	[[Category: ~~Hou, J~~]]	+	[[Category: Csgid]]
-	[[Category: ~~Anderson, W.F~~]]	+	[[Category: Fabg]]
-	[[Category: ~~Center For Structural Genomics Of Infectious Diseases (Csgid)~~]]	+	[[Category: Oxidoreductase]]
-	[[Category: ~~Cooper, D.R~~]]	+	[[Category: Vibrio cholerae]]

OCA: Protected "5end" [edit=sysop:move=sysop]

2015-12-01T03:05:49Z

Protected "5end" [edit=sysop:move=sysop]

←Older revision

Revision as of 03:05, 1 December 2015

OCA: New page: '''Unreleased structure''' The entry 5end is ON HOLD Authors: Hou, J., Cooper, D.R., Zheng, H., Anderson, W.F., Minor, W., Center for Structural Genomics of Infectious Diseases (CSGID) ...

2015-12-01T03:05:47Z

New page: '''Unreleased structure''' The entry 5end is ON HOLD Authors: Hou, J., Cooper, D.R., Zheng, H., Anderson, W.F., Minor, W., Center for Structural Genomics of Infectious Diseases (CSGID) ...

New page

'''Unreleased structure'''

The entry 5end is ON HOLD

Authors: Hou, J., Cooper, D.R., Zheng, H., Anderson, W.F., Minor, W., Center for Structural Genomics of Infectious Diseases (CSGID)

Description: Crystal structure of beta-ketoacyl-acyl carrier protein reductase (FabG)(Q152A) from Vibrio cholerae
[[Category: Unreleased Structures]]
[[Category: Zheng, H]]
[[Category: Minor, W]]
[[Category: Hou, J]]
[[Category: Anderson, W.F]]
[[Category: Center For Structural Genomics Of Infectious Diseases (Csgid)]]
[[Category: Cooper, D.R]]